Rabbit Polyclonal CPL1 antibody. Suitable for WB and reacts with Caenorhabditis elegans samples. Cited in 32 publications.
Constituents: Whole serum
| WB | |
|---|---|
| Caenorhabditis elegans | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Caenorhabditis elegans | Dilution info 1/200.00000 - 1/1000.00000 | Notes - |
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Cysteine protease which plays an essential role in the degradation of proteins in lysosomes (PubMed:15456850, PubMed:24829385). During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome-like structure where a slow and controlled degradation of yolk proteins occurs (PubMed:15456850, PubMed:24829385). In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes (PubMed:24829385). In embryos, required for the degradation of endocytic and autophagic cargos (PubMed:24829385). In embryos, may play a role in the degradation of lipid-containing droplets (PubMed:26773047). Required for larval development (PubMed:11707440, PubMed:15456850).
T03E6.7, cpl-1, Cathepsin L-like
Rabbit Polyclonal CPL1 antibody. Suitable for WB and reacts with Caenorhabditis elegans samples. Cited in 32 publications.
Constituents: Whole serum
Reacts specifically with Cathepsin L/MEP protease 36 kDa wild type protein of C.elegans
Cathepsin L also known as CTSL is a protease enzyme that has a mass of approximately 29-30 kDa. It originates from the peptidase C1 family and undergoes activation in acidic environments. This protein carries out proteolytic processes by breaking down proteins through cleaving peptide bonds. Cathepsin L has various forms including MEP (a common alternate name) and MEP L and it expresses itself in organs such as the liver kidney and spleen as well as in tumors and immune cells. It has a significant functional role in lysosomes where it degrades proteins.
Cathepsin L links to cellular homeostasis and extracellular matrix remodeling. It often acts in protein turnover and antigen processing within endolysosomal compartments making it essential for major histocompatibility complex class II presentation. Cathepsin L forms complexes in certain conditions playing roles in interacting and modifying other proteins. It controls processes essential for cell survival differentiation and apoptosis.
Cathepsin L plays significant roles in pathways like apoptosis and autophagy. It coordinates with other proteases and proteins such as cathepsin B and cathepsin S to regulate cell death and survival. In apoptosis cathepsin L mediates the breakdown of cellular components working alongside caspases. Its interaction with autophagy involves degradation of long-lived proteins highlighting its role in recycling amino acids during stress conditions.
Cathepsin L connects strongly to cancer and fibrotic diseases. It contributes to tumor progression and metastasis due to its ability to degrade the extracellular matrix and enable cancer cell invasion. In fibrosis cathepsin L modulates the turnover of fibrous tissue linking to the development of lung fibrotic diseases. Proteins like collagenases work in concert with cathepsin L during these pathological processes to remodel tissues underlining its implication in disease states.
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